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Published online
doi:10.1083/jcb.200707123
The Journal of Cell Biology
The Rockefeller University Press, 0021-9525 $30.00
© Bihlmaier et al.
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The disulfide relay system of mitochondria is connected to the respiratory chain



Karl Bihlmaier1, Nikola Mesecke1,2, Nadia Terziyska2, Melanie Bien1, Kai Hell2, and Johannes M. Herrmann1

1 Department of Cell Biology, University of Kaiserslautern, Kaiserslautern 67663, Germany
2 Department of Physiological Chemistry, University of Munich, Munich 81377, Germany

Correspondence to J.M. Herrmann: hannes.herrmann{at}biologie.uni-kl.de

All proteins of the intermembrane space of mitochondria are encoded by nuclear genes and synthesized in the cytosol. Many of these proteins lack presequences but are imported into mitochondria in an oxidation-driven process that relies on the activity of Mia40 and Erv1. Both factors form a disulfide relay system in which Mia40 functions as a receptor that transiently interacts with incoming polypeptides via disulfide bonds. Erv1 is a sulfhydryl oxidase that oxidizes and activates Mia40, but it has remained unclear how Erv1 itself is oxidized. Here, we show that Erv1 passes its electrons on to molecular oxygen via interaction with cytochrome c and cytochrome c oxidase. This connection to the respiratory chain increases the efficient oxidation of the relay system in mitochondria and prevents the formation of toxic hydrogen peroxide. Thus, analogous to the system in the bacterial periplasm, the disulfide relay in the intermembrane space is connected to the electron transport chain of the inner membrane.

Abbreviations used in this paper: ALR, augmenter of liver regeneration; IMS, intermembrane space.


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